dystrophin isoform X3 [Chiloscyllium plagiosum]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| EFh_DMD | cd16246 | EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ... |
3221-3382 | 9.57e-114 | |||||
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection. : Pssm-ID: 320004 Cd Length: 162 Bit Score: 358.19 E-value: 9.57e-114
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| CH_DMD_rpt2 | cd21233 | second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
153-263 | 2.88e-66 | |||||
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain. : Pssm-ID: 409082 Cd Length: 111 Bit Score: 220.19 E-value: 2.88e-66
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| CH_DMD_rpt1 | cd21231 | first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
28-138 | 4.01e-66 | |||||
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain. : Pssm-ID: 409080 Cd Length: 111 Bit Score: 219.79 E-value: 4.01e-66
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| ZZ_dystrophin | cd02334 | Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ... |
3407-3455 | 1.13e-29 | |||||
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan. : Pssm-ID: 239074 Cd Length: 49 Bit Score: 113.22 E-value: 1.13e-29
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
351-569 | 1.13e-26 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 110.61 E-value: 1.13e-26
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2778-3019 | 5.43e-20 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 91.35 E-value: 5.43e-20
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1060-1274 | 7.31e-20 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 90.97 E-value: 7.31e-20
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2204-2419 | 1.96e-18 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 86.73 E-value: 1.96e-18
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
473-679 | 2.86e-15 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 77.49 E-value: 2.86e-15
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2558-2763 | 1.11e-14 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.95 E-value: 1.11e-14
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
733-937 | 2.65e-14 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 74.79 E-value: 2.65e-14
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1279-1490 | 1.61e-11 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 66.70 E-value: 1.61e-11
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3021-3131 | 2.67e-09 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 2.67e-09
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1909-2066 | 2.79e-09 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here : Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 2.79e-09
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1696-1793 | 2.45e-07 | |||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. : Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.55 E-value: 2.45e-07
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
3145-3184 | 6.14e-06 | |||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. : Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 45.21 E-value: 6.14e-06
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| SPEC super family | cl02488 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1512-1693 | 1.33e-05 | |||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here The actual alignment was detected with superfamily member cd00176: Pssm-ID: 413338 [Multi-domain] Cd Length: 213 Bit Score: 48.98 E-value: 1.33e-05
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| Name | Accession | Description | Interval | E-value | |||||||||||
| EFh_DMD | cd16246 | EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ... |
3221-3382 | 9.57e-114 | |||||||||||
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection. Pssm-ID: 320004 Cd Length: 162 Bit Score: 358.19 E-value: 9.57e-114
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| CH_DMD_rpt2 | cd21233 | second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
153-263 | 2.88e-66 | |||||||||||
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain. Pssm-ID: 409082 Cd Length: 111 Bit Score: 220.19 E-value: 2.88e-66
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| CH_DMD_rpt1 | cd21231 | first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
28-138 | 4.01e-66 | |||||||||||
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain. Pssm-ID: 409080 Cd Length: 111 Bit Score: 219.79 E-value: 4.01e-66
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| EF-hand_2 | pfam09068 | EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ... |
3185-3303 | 9.56e-58 | |||||||||||
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding. Pssm-ID: 462668 Cd Length: 123 Bit Score: 196.22 E-value: 9.56e-58
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| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
29-249 | 8.53e-37 | |||||||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 150.09 E-value: 8.53e-37
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| ZZ_dystrophin | cd02334 | Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ... |
3407-3455 | 1.13e-29 | |||||||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan. Pssm-ID: 239074 Cd Length: 49 Bit Score: 113.22 E-value: 1.13e-29
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
351-569 | 1.13e-26 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 110.61 E-value: 1.13e-26
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
153-257 | 3.04e-21 | |||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 91.19 E-value: 3.04e-21
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
155-252 | 9.99e-21 | |||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 89.68 E-value: 9.99e-21
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
32-136 | 3.73e-20 | |||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 88.11 E-value: 3.73e-20
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2778-3019 | 5.43e-20 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 91.35 E-value: 5.43e-20
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1060-1274 | 7.31e-20 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 90.97 E-value: 7.31e-20
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
36-134 | 4.88e-19 | |||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 84.67 E-value: 4.88e-19
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2204-2419 | 1.96e-18 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 86.73 E-value: 1.96e-18
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
3403-3448 | 2.17e-16 | |||||||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 75.21 E-value: 2.17e-16
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
473-679 | 2.86e-15 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 77.49 E-value: 2.86e-15
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2558-2763 | 1.11e-14 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.95 E-value: 1.11e-14
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
733-937 | 2.65e-14 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 74.79 E-value: 2.65e-14
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
3404-3447 | 3.60e-14 | |||||||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 69.00 E-value: 3.60e-14
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
351-458 | 2.43e-12 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 65.80 E-value: 2.43e-12
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| SPEC | smart00150 | Spectrin repeats; |
355-456 | 2.60e-12 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 65.43 E-value: 2.60e-12
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1279-1490 | 1.61e-11 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 66.70 E-value: 1.61e-11
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1062-1163 | 3.93e-11 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 62.34 E-value: 3.93e-11
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3021-3131 | 2.67e-09 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 2.67e-09
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1909-2066 | 2.79e-09 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 2.79e-09
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2203-2308 | 5.56e-09 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 56.17 E-value: 5.56e-09
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| SPEC | smart00150 | Spectrin repeats; |
2561-2662 | 2.10e-08 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 54.64 E-value: 2.10e-08
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| SPEC | smart00150 | Spectrin repeats; |
1062-1164 | 3.25e-08 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.87 E-value: 3.25e-08
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| SPEC | smart00150 | Spectrin repeats; |
2206-2307 | 3.69e-08 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.87 E-value: 3.69e-08
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3020-3126 | 6.15e-08 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 53.48 E-value: 6.15e-08
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| SPEC | smart00150 | Spectrin repeats; |
733-838 | 1.05e-07 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 52.33 E-value: 1.05e-07
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1696-1793 | 2.45e-07 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.55 E-value: 2.45e-07
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1142-1816 | 3.96e-07 | |||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 3.96e-07
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| SPEC | smart00150 | Spectrin repeats; |
2778-2887 | 4.42e-07 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.79 E-value: 4.42e-07
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| SPEC | smart00150 | Spectrin repeats; |
1978-2066 | 1.29e-06 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 1.29e-06
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
3145-3184 | 6.14e-06 | |||||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 45.21 E-value: 6.14e-06
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1976-2058 | 6.89e-06 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 47.31 E-value: 6.89e-06
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| SPEC | smart00150 | Spectrin repeats; |
3024-3124 | 7.67e-06 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 7.67e-06
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1030-1366 | 1.03e-05 | |||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.03e-05
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
733-838 | 1.06e-05 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 46.93 E-value: 1.06e-05
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1512-1693 | 1.33e-05 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 48.98 E-value: 1.33e-05
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
3142-3184 | 2.99e-05 | |||||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 43.36 E-value: 2.99e-05
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
1046-1602 | 3.80e-05 | |||||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.80e-05
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
3146-3182 | 1.22e-04 | |||||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 41.72 E-value: 1.22e-04
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| HEC1 | COG5185 | Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1161-1490 | 1.97e-04 | |||||||||||
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.26 E-value: 1.97e-04
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| SPEC | smart00150 | Spectrin repeats; |
1281-1377 | 2.21e-04 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.09 E-value: 2.21e-04
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2778-2877 | 3.68e-04 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 42.69 E-value: 3.68e-04
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1632-1793 | 4.72e-04 | |||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.36 E-value: 4.72e-04
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1299-1606 | 9.38e-04 | |||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 9.38e-04
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2826-3130 | 1.43e-03 | |||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.43e-03
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1286-1378 | 1.60e-03 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 40.76 E-value: 1.60e-03
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
1875-2077 | 2.75e-03 | |||||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.75e-03
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2567-2663 | 2.80e-03 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.99 E-value: 2.80e-03
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| SPEC | smart00150 | Spectrin repeats; |
573-671 | 2.97e-03 | |||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.97e-03
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1591-1693 | 4.02e-03 | |||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.61 E-value: 4.02e-03
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| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2572-2728 | 4.84e-03 | |||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.84e-03
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| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
2587-2732 | 6.28e-03 | |||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 6.28e-03
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| PRK10929 | PRK10929 | putative mechanosensitive channel protein; Provisional |
1293-1438 | 6.85e-03 | |||||||||||
putative mechanosensitive channel protein; Provisional Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 6.85e-03
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| Name | Accession | Description | Interval | E-value | |||||||||||||
| EFh_DMD | cd16246 | EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ... |
3221-3382 | 9.57e-114 | |||||||||||||
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection. Pssm-ID: 320004 Cd Length: 162 Bit Score: 358.19 E-value: 9.57e-114
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| EFh_DMD_like | cd16242 | EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ... |
3221-3382 | 2.62e-103 | |||||||||||||
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils. Pssm-ID: 320000 Cd Length: 163 Bit Score: 328.43 E-value: 2.62e-103
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| EFh_UTRO | cd16247 | EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ... |
3222-3382 | 8.14e-89 | |||||||||||||
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. Pssm-ID: 320005 Cd Length: 162 Bit Score: 286.79 E-value: 8.14e-89
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| EFh_DRP-2 | cd16248 | EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ... |
3221-3381 | 4.09e-84 | |||||||||||||
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises only two spectrin repeats (SRs) and a WW domain. Pssm-ID: 320006 Cd Length: 162 Bit Score: 273.21 E-value: 4.09e-84
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| CH_DMD_rpt2 | cd21233 | second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
153-263 | 2.88e-66 | |||||||||||||
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain. Pssm-ID: 409082 Cd Length: 111 Bit Score: 220.19 E-value: 2.88e-66
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| CH_DMD_rpt1 | cd21231 | first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
28-138 | 4.01e-66 | |||||||||||||
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain. Pssm-ID: 409080 Cd Length: 111 Bit Score: 219.79 E-value: 4.01e-66
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| EFh_DMD_DYTN_DTN | cd15901 | EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ... |
3222-3381 | 1.26e-65 | |||||||||||||
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize. Pssm-ID: 319999 Cd Length: 163 Bit Score: 220.22 E-value: 1.26e-65
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| CH_DMD-like_rpt1 | cd21186 | first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
32-138 | 6.93e-61 | |||||||||||||
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409035 Cd Length: 107 Bit Score: 204.54 E-value: 6.93e-61
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| EF-hand_2 | pfam09068 | EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ... |
3185-3303 | 9.56e-58 | |||||||||||||
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding. Pssm-ID: 462668 Cd Length: 123 Bit Score: 196.22 E-value: 9.56e-58
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| CH_UTRN_rpt1 | cd21232 | first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
32-138 | 3.91e-57 | |||||||||||||
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain. Pssm-ID: 409081 Cd Length: 107 Bit Score: 193.69 E-value: 3.91e-57
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| CH_DMD-like_rpt2 | cd21187 | second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
153-257 | 1.54e-55 | |||||||||||||
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409036 Cd Length: 104 Bit Score: 189.18 E-value: 1.54e-55
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| CH_UTRN_rpt2 | cd21234 | second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
153-257 | 2.03e-52 | |||||||||||||
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain. Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 180.15 E-value: 2.03e-52
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| EF-hand_3 | pfam09069 | EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ... |
3307-3398 | 3.07e-49 | |||||||||||||
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding. Pssm-ID: 462669 Cd Length: 90 Bit Score: 170.56 E-value: 3.07e-49
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| CH_PLEC-like_rpt2 | cd21189 | second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
152-257 | 2.32e-41 | |||||||||||||
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409038 Cd Length: 105 Bit Score: 148.69 E-value: 2.32e-41
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| CH_PLEC-like_rpt1 | cd21188 | first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
33-136 | 2.79e-41 | |||||||||||||
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409037 Cd Length: 105 Bit Score: 148.32 E-value: 2.79e-41
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| CH_SPTB-like_rpt1 | cd21246 | first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
23-133 | 1.34e-40 | |||||||||||||
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409095 Cd Length: 117 Bit Score: 147.13 E-value: 1.34e-40
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| CH_beta_spectrin_rpt2 | cd21194 | second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
157-253 | 1.40e-37 | |||||||||||||
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409043 Cd Length: 105 Bit Score: 137.93 E-value: 1.40e-37
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| CH_SPTB_like_rpt2 | cd21248 | second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
157-253 | 4.21e-37 | |||||||||||||
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409097 Cd Length: 105 Bit Score: 136.37 E-value: 4.21e-37
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| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
29-249 | 8.53e-37 | |||||||||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 150.09 E-value: 8.53e-37
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| CH_beta_spectrin_rpt1 | cd21193 | first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
23-133 | 9.99e-37 | |||||||||||||
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409042 Cd Length: 116 Bit Score: 135.89 E-value: 9.99e-37
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| CH_SPTB_rpt2 | cd21319 | second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
149-254 | 1.88e-36 | |||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409168 Cd Length: 112 Bit Score: 135.13 E-value: 1.88e-36
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| CH_SPTBN4_rpt1 | cd21318 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
23-133 | 5.40e-36 | |||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409167 Cd Length: 139 Bit Score: 134.77 E-value: 5.40e-36
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| CH_SPTBN2_rpt1 | cd21317 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
23-133 | 8.86e-36 | |||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409166 Cd Length: 132 Bit Score: 133.64 E-value: 8.86e-36
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| CH_SYNE1_rpt1 | cd21241 | first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
29-138 | 1.07e-35 | |||||||||||||
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409090 Cd Length: 113 Bit Score: 132.88 E-value: 1.07e-35
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| CH_DYST_rpt1 | cd21236 | first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
19-140 | 3.96e-34 | |||||||||||||
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409085 Cd Length: 128 Bit Score: 128.95 E-value: 3.96e-34
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| CH_SYNE2_rpt1 | cd21242 | first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
29-138 | 9.93e-33 | |||||||||||||
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409091 Cd Length: 111 Bit Score: 124.17 E-value: 9.93e-33
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| CH_SPTBN5_rpt2 | cd21249 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
150-253 | 3.48e-32 | |||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409098 Cd Length: 109 Bit Score: 122.66 E-value: 3.48e-32
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| CH_PLEC_rpt1 | cd21235 | first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
28-141 | 2.09e-31 | |||||||||||||
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409084 Cd Length: 119 Bit Score: 120.90 E-value: 2.09e-31
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| CH_SYNE-like_rpt1 | cd21190 | first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
29-138 | 4.59e-31 | |||||||||||||
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409039 Cd Length: 113 Bit Score: 119.60 E-value: 4.59e-31
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| CH_ACTN_rpt1 | cd21214 | first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
31-133 | 5.99e-31 | |||||||||||||
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409063 Cd Length: 105 Bit Score: 119.03 E-value: 5.99e-31
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| CH_SYNE1_rpt2 | cd21243 | second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
150-257 | 8.32e-31 | |||||||||||||
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409092 Cd Length: 109 Bit Score: 118.57 E-value: 8.32e-31
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| CH_SPTBN4_rpt2 | cd21322 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
147-254 | 1.80e-30 | |||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409171 Cd Length: 130 Bit Score: 118.62 E-value: 1.80e-30
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| CH_ACTN_rpt2 | cd21216 | second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
147-255 | 5.74e-30 | |||||||||||||
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409065 Cd Length: 115 Bit Score: 116.31 E-value: 5.74e-30
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| ZZ_dystrophin | cd02334 | Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ... |
3407-3455 | 1.13e-29 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan. Pssm-ID: 239074 Cd Length: 49 Bit Score: 113.22 E-value: 1.13e-29
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| CH_DYST_rpt2 | cd21239 | second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
151-257 | 1.98e-29 | |||||||||||||
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409088 Cd Length: 104 Bit Score: 114.70 E-value: 1.98e-29
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| CH_SPTBN1_rpt1 | cd21316 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
23-133 | 2.55e-29 | |||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409165 Cd Length: 154 Bit Score: 116.30 E-value: 2.55e-29
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| CH_SYNE-like_rpt2 | cd21192 | second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
150-257 | 2.75e-29 | |||||||||||||
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409041 Cd Length: 107 Bit Score: 114.44 E-value: 2.75e-29
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| CH_CLMN_rpt1 | cd21191 | first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
29-138 | 2.75e-29 | |||||||||||||
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409040 Cd Length: 114 Bit Score: 114.60 E-value: 2.75e-29
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| CH_SPTBN2_rpt2 | cd21321 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
149-254 | 4.72e-29 | |||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409170 Cd Length: 119 Bit Score: 114.00 E-value: 4.72e-29
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| CH_SPTBN1_rpt2 | cd21320 | second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
152-254 | 7.17e-29 | |||||||||||||
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409169 Cd Length: 108 Bit Score: 113.27 E-value: 7.17e-29
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| CH_MACF1_rpt1 | cd21237 | first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
28-140 | 8.34e-29 | |||||||||||||
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409086 Cd Length: 118 Bit Score: 113.20 E-value: 8.34e-29
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| CH_SpAIN1-like_rpt1 | cd21215 | first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
31-133 | 1.51e-28 | |||||||||||||
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409064 Cd Length: 107 Bit Score: 112.11 E-value: 1.51e-28
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| CH_PLEC_rpt2 | cd21238 | second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
151-257 | 2.11e-28 | |||||||||||||
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409087 Cd Length: 106 Bit Score: 111.65 E-value: 2.11e-28
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| CH_jitterbug-like_rpt1 | cd21227 | first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
32-137 | 2.17e-27 | |||||||||||||
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409076 Cd Length: 109 Bit Score: 108.91 E-value: 2.17e-27
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| CH_CTX_rpt2 | cd21226 | second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
153-253 | 2.62e-27 | |||||||||||||
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409075 Cd Length: 103 Bit Score: 108.32 E-value: 2.62e-27
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| CH_MICALL2 | cd21253 | calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
155-256 | 6.58e-27 | |||||||||||||
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409102 Cd Length: 106 Bit Score: 107.43 E-value: 6.58e-27
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
351-569 | 1.13e-26 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 110.61 E-value: 1.13e-26
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| CH_MICAL_EHBP-like | cd22198 | calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
157-256 | 3.00e-26 | |||||||||||||
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409188 Cd Length: 105 Bit Score: 105.45 E-value: 3.00e-26
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| CH_MACF1_rpt2 | cd21240 | second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
154-257 | 1.37e-25 | |||||||||||||
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409089 Cd Length: 107 Bit Score: 103.58 E-value: 1.37e-25
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| CH_SYNE2_rpt2 | cd21244 | second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
150-254 | 1.17e-24 | |||||||||||||
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409093 Cd Length: 109 Bit Score: 101.06 E-value: 1.17e-24
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| CH_MICALL | cd21197 | calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
155-253 | 1.60e-23 | |||||||||||||
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409046 Cd Length: 105 Bit Score: 97.61 E-value: 1.60e-23
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| CH_SpAIN1-like_rpt2 | cd21291 | second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
157-253 | 2.01e-23 | |||||||||||||
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409140 Cd Length: 115 Bit Score: 97.98 E-value: 2.01e-23
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| CH_SPTBN5_rpt1 | cd21247 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
23-137 | 3.51e-23 | |||||||||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409096 Cd Length: 125 Bit Score: 97.52 E-value: 3.51e-23
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| CH_SMTN-like | cd21200 | calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
156-256 | 4.26e-22 | |||||||||||||
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409049 Cd Length: 107 Bit Score: 93.56 E-value: 4.26e-22
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| CH_ACTN4_rpt2 | cd21290 | second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
147-256 | 8.76e-22 | |||||||||||||
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409139 Cd Length: 125 Bit Score: 93.61 E-value: 8.76e-22
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| CH_EHBP | cd21198 | calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
152-252 | 1.51e-21 | |||||||||||||
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409047 Cd Length: 105 Bit Score: 92.10 E-value: 1.51e-21
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| CH_ACTN1_rpt2 | cd21287 | second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
147-256 | 2.18e-21 | |||||||||||||
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409136 Cd Length: 124 Bit Score: 92.46 E-value: 2.18e-21
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| CH_dFLNA-like_rpt1 | cd21311 | first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
33-137 | 2.98e-21 | |||||||||||||
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409160 Cd Length: 124 Bit Score: 92.13 E-value: 2.98e-21
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
153-257 | 3.04e-21 | |||||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 91.19 E-value: 3.04e-21
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
155-252 | 9.99e-21 | |||||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 89.68 E-value: 9.99e-21
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| CH_FLN-like_rpt1 | cd21183 | first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
33-135 | 1.03e-20 | |||||||||||||
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409032 Cd Length: 108 Bit Score: 89.85 E-value: 1.03e-20
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| CH_FLN-like_rpt2 | cd21184 | second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
153-251 | 3.02e-20 | |||||||||||||
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409033 Cd Length: 103 Bit Score: 88.45 E-value: 3.02e-20
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
32-136 | 3.73e-20 | |||||||||||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 88.11 E-value: 3.73e-20
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| CH_ACTN3_rpt2 | cd21289 | second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
147-256 | 4.64e-20 | |||||||||||||
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409138 Cd Length: 124 Bit Score: 88.63 E-value: 4.64e-20
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| CH_SMTNL1 | cd21260 | calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
153-259 | 5.15e-20 | |||||||||||||
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409109 Cd Length: 116 Bit Score: 88.22 E-value: 5.15e-20
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2778-3019 | 5.43e-20 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 91.35 E-value: 5.43e-20
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| CH_MICALL1 | cd21252 | calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
157-253 | 6.57e-20 | |||||||||||||
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409101 Cd Length: 107 Bit Score: 87.62 E-value: 6.57e-20
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1060-1274 | 7.31e-20 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 90.97 E-value: 7.31e-20
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| CH_EHBP1 | cd21254 | calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
152-255 | 7.77e-20 | |||||||||||||
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409103 Cd Length: 107 Bit Score: 87.21 E-value: 7.77e-20
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| EFh_DAH | cd16245 | EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ... |
3229-3381 | 1.08e-19 | |||||||||||||
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Pssm-ID: 320003 [Multi-domain] Cd Length: 164 Bit Score: 88.89 E-value: 1.08e-19
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| CH_FLN_rpt1 | cd21228 | first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
33-135 | 1.45e-19 | |||||||||||||
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409077 Cd Length: 108 Bit Score: 86.39 E-value: 1.45e-19
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| CH_CLMN_rpt2 | cd21245 | second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
155-257 | 2.45e-19 | |||||||||||||
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409094 Cd Length: 106 Bit Score: 86.00 E-value: 2.45e-19
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
36-134 | 4.88e-19 | |||||||||||||
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p. Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 84.67 E-value: 4.88e-19
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| CH_SMTNB | cd21259 | calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
154-259 | 5.28e-19 | |||||||||||||
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409108 Cd Length: 112 Bit Score: 85.04 E-value: 5.28e-19
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| CH_ACTN2_rpt2 | cd21288 | second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
147-256 | 1.07e-18 | |||||||||||||
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409137 Cd Length: 124 Bit Score: 84.74 E-value: 1.07e-18
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2204-2419 | 1.96e-18 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 86.73 E-value: 1.96e-18
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| CH_MICAL2_3-like | cd21195 | calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
157-256 | 2.32e-18 | |||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 83.17 E-value: 2.32e-18
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| EFh_DTN | cd16244 | EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ... |
3227-3381 | 9.37e-18 | |||||||||||||
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrobrevins contain one or two syntrophin binding sites (SBSs). Pssm-ID: 320002 [Multi-domain] Cd Length: 161 Bit Score: 83.06 E-value: 9.37e-18
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| CH_MICAL3 | cd21251 | calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
157-256 | 1.42e-17 | |||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 81.15 E-value: 1.42e-17
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| CH_NAV2-like | cd21212 | calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
34-134 | 1.48e-16 | |||||||||||||
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. Pssm-ID: 409061 Cd Length: 105 Bit Score: 78.01 E-value: 1.48e-16
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| CH_EHBP1L1 | cd21255 | calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
157-252 | 1.52e-16 | |||||||||||||
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409104 Cd Length: 105 Bit Score: 77.91 E-value: 1.52e-16
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| CH_CYTS | cd21199 | calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
157-254 | 1.57e-16 | |||||||||||||
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409048 Cd Length: 112 Bit Score: 78.17 E-value: 1.57e-16
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| CH_SMTNA | cd21258 | calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
154-256 | 2.14e-16 | |||||||||||||
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409107 Cd Length: 111 Bit Score: 77.78 E-value: 2.14e-16
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
3403-3448 | 2.17e-16 | |||||||||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 75.21 E-value: 2.17e-16
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| CH_SMTNL2 | cd21261 | calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
154-256 | 2.18e-16 | |||||||||||||
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409110 Cd Length: 107 Bit Score: 77.31 E-value: 2.18e-16
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| CH_MICAL2 | cd21250 | calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
157-255 | 1.65e-15 | |||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 74.92 E-value: 1.65e-15
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| CH_FLNC_rpt1 | cd21310 | first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
33-137 | 1.94e-15 | |||||||||||||
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409159 Cd Length: 125 Bit Score: 75.45 E-value: 1.94e-15
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
473-679 | 2.86e-15 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 77.49 E-value: 2.86e-15
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| CH_PLS_FIM_rpt3 | cd21219 | third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
27-134 | 3.85e-15 | |||||||||||||
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409068 Cd Length: 113 Bit Score: 74.24 E-value: 3.85e-15
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| CH_CTX_rpt1 | cd21225 | first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
31-131 | 5.23e-15 | |||||||||||||
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409074 Cd Length: 111 Bit Score: 73.72 E-value: 5.23e-15
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2892-3128 | 7.42e-15 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 76.33 E-value: 7.42e-15
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2104-2309 | 9.32e-15 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.95 E-value: 9.32e-15
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2558-2763 | 1.11e-14 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.95 E-value: 1.11e-14
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
733-937 | 2.65e-14 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 74.79 E-value: 2.65e-14
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
3404-3447 | 3.60e-14 | |||||||||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 69.00 E-value: 3.60e-14
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| CH_SF | cd00014 | calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
35-133 | 5.11e-14 | |||||||||||||
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav). Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 70.45 E-value: 5.11e-14
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| CH_FLNB_rpt1 | cd21309 | first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
31-137 | 1.16e-13 | |||||||||||||
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409158 Cd Length: 131 Bit Score: 70.49 E-value: 1.16e-13
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| CH_FLNA_rpt1 | cd21308 | first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
21-137 | 1.70e-13 | |||||||||||||
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409157 Cd Length: 129 Bit Score: 70.11 E-value: 1.70e-13
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| CH_jitterbug-like_rpt2 | cd21229 | second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
153-250 | 2.25e-13 | |||||||||||||
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409078 Cd Length: 105 Bit Score: 68.95 E-value: 2.25e-13
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| CH_PLS_rpt3 | cd21298 | third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
29-129 | 7.36e-13 | |||||||||||||
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409147 Cd Length: 117 Bit Score: 67.65 E-value: 7.36e-13
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| CH_CYTSB | cd21257 | calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
157-254 | 1.41e-12 | |||||||||||||
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409106 Cd Length: 112 Bit Score: 66.98 E-value: 1.41e-12
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
954-1167 | 1.55e-12 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.78 E-value: 1.55e-12
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| CH_FIMB_rpt3 | cd21300 | third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
29-129 | 2.43e-12 | |||||||||||||
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409149 Cd Length: 119 Bit Score: 66.29 E-value: 2.43e-12
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
351-458 | 2.43e-12 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 65.80 E-value: 2.43e-12
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| SPEC | smart00150 | Spectrin repeats; |
355-456 | 2.60e-12 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 65.43 E-value: 2.60e-12
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| CH_CYTSA | cd21256 | calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
157-254 | 2.72e-12 | |||||||||||||
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409105 Cd Length: 119 Bit Score: 66.25 E-value: 2.72e-12
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1279-1490 | 1.61e-11 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 66.70 E-value: 1.61e-11
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| CH_SF | cd00014 | calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
154-252 | 1.95e-11 | |||||||||||||
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav). Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 63.13 E-value: 1.95e-11
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| EFh_DTNB | cd16250 | EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ... |
3227-3381 | 1.99e-11 | |||||||||||||
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs). Pssm-ID: 320008 Cd Length: 161 Bit Score: 65.05 E-value: 1.99e-11
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| CH_FLN_rpt2 | cd21230 | second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
157-250 | 2.88e-11 | |||||||||||||
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409079 Cd Length: 103 Bit Score: 62.79 E-value: 2.88e-11
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1062-1163 | 3.93e-11 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 62.34 E-value: 3.93e-11
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| EFh_DYTN | cd16243 | EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ... |
3250-3382 | 1.44e-10 | |||||||||||||
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize. Pssm-ID: 320001 Cd Length: 163 Bit Score: 62.40 E-value: 1.44e-10
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| EFh_DTNA | cd16249 | EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ... |
3256-3363 | 4.68e-10 | |||||||||||||
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, alpha-dystrobrevin contain two syntrophin binding sites (SBSs). Pssm-ID: 320007 Cd Length: 161 Bit Score: 61.07 E-value: 4.68e-10
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| CH_PLS_FIM_rpt1 | cd21217 | first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
35-132 | 7.78e-10 | |||||||||||||
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 59.12 E-value: 7.78e-10
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| CH_DIXDC1 | cd21213 | calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
34-134 | 1.55e-09 | |||||||||||||
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409062 Cd Length: 107 Bit Score: 58.08 E-value: 1.55e-09
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| CH_PLS_FIM_rpt2 | cd21218 | second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
153-254 | 1.63e-09 | |||||||||||||
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409067 Cd Length: 114 Bit Score: 58.08 E-value: 1.63e-09
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| CH_AtFIM_like_rpt3 | cd21299 | third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
28-134 | 2.01e-09 | |||||||||||||
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409148 Cd Length: 114 Bit Score: 57.90 E-value: 2.01e-09
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3021-3131 | 2.67e-09 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 2.67e-09
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1909-2066 | 2.79e-09 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 2.79e-09
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| CH_NAV3 | cd21286 | calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
36-131 | 4.12e-09 | |||||||||||||
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409135 Cd Length: 105 Bit Score: 56.58 E-value: 4.12e-09
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| CH_ASPM_rpt1 | cd21223 | first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
51-132 | 4.26e-09 | |||||||||||||
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409072 Cd Length: 113 Bit Score: 56.83 E-value: 4.26e-09
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
571-838 | 4.27e-09 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 59.38 E-value: 4.27e-09
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2203-2308 | 5.56e-09 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 56.17 E-value: 5.56e-09
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| CH_MICAL1 | cd21196 | calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
157-250 | 7.02e-09 | |||||||||||||
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409045 Cd Length: 106 Bit Score: 56.21 E-value: 7.02e-09
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| SPEC | smart00150 | Spectrin repeats; |
2561-2662 | 2.10e-08 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 54.64 E-value: 2.10e-08
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| SPEC | smart00150 | Spectrin repeats; |
1062-1164 | 3.25e-08 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.87 E-value: 3.25e-08
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| SPEC | smart00150 | Spectrin repeats; |
2206-2307 | 3.69e-08 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.87 E-value: 3.69e-08
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
474-567 | 3.71e-08 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 53.86 E-value: 3.71e-08
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3020-3126 | 6.15e-08 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 53.48 E-value: 6.15e-08
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| CCDC158 | pfam15921 | Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
986-1776 | 6.33e-08 | |||||||||||||
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known. Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 6.33e-08
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| SPEC | smart00150 | Spectrin repeats; |
733-838 | 1.05e-07 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 52.33 E-value: 1.05e-07
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| SPEC | smart00150 | Spectrin repeats; |
473-566 | 1.53e-07 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.95 E-value: 1.53e-07
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| CH_PARV_rpt2 | cd21222 | second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
17-134 | 2.36e-07 | |||||||||||||
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409071 Cd Length: 121 Bit Score: 52.20 E-value: 2.36e-07
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1696-1793 | 2.45e-07 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.55 E-value: 2.45e-07
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| ZZ | cd02249 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
3409-3455 | 2.62e-07 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 49.74 E-value: 2.62e-07
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| CH_PLS3_rpt3 | cd21331 | third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
29-132 | 3.84e-07 | |||||||||||||
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409180 Cd Length: 134 Bit Score: 51.92 E-value: 3.84e-07
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1142-1816 | 3.96e-07 | |||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 3.96e-07
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| SPEC | smart00150 | Spectrin repeats; |
2778-2887 | 4.42e-07 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.79 E-value: 4.42e-07
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| CH_FLNC_rpt2 | cd21314 | second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
149-252 | 1.10e-06 | |||||||||||||
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409163 Cd Length: 115 Bit Score: 50.07 E-value: 1.10e-06
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| CH_ASPM_rpt2 | cd21224 | second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
157-256 | 1.18e-06 | |||||||||||||
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 50.76 E-value: 1.18e-06
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| SPEC | smart00150 | Spectrin repeats; |
1978-2066 | 1.29e-06 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 1.29e-06
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| CH_FIMB_rpt1 | cd21294 | first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
31-132 | 1.66e-06 | |||||||||||||
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409143 Cd Length: 125 Bit Score: 49.75 E-value: 1.66e-06
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| CH_NAV2 | cd21285 | calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
34-131 | 1.66e-06 | |||||||||||||
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409134 Cd Length: 121 Bit Score: 49.58 E-value: 1.66e-06
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| CH_dFLNA-like_rpt2 | cd21315 | second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
157-250 | 1.78e-06 | |||||||||||||
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409164 Cd Length: 118 Bit Score: 49.39 E-value: 1.78e-06
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1175-1274 | 2.60e-06 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 48.47 E-value: 2.60e-06
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1105-1444 | 4.51e-06 | |||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 4.51e-06
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
3145-3184 | 6.14e-06 | |||||||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 45.21 E-value: 6.14e-06
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| SPEC | smart00150 | Spectrin repeats; |
2895-3016 | 6.31e-06 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 6.31e-06
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| ZZ_PCMF_like | cd02338 | Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ... |
3409-3452 | 6.47e-06 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination. Pssm-ID: 239078 Cd Length: 49 Bit Score: 45.80 E-value: 6.47e-06
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1976-2058 | 6.89e-06 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 47.31 E-value: 6.89e-06
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| SPEC | smart00150 | Spectrin repeats; |
3024-3124 | 7.67e-06 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 7.67e-06
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| CH_PLS_FIM_rpt2 | cd21218 | second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
40-131 | 9.76e-06 | |||||||||||||
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409067 Cd Length: 114 Bit Score: 47.29 E-value: 9.76e-06
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1030-1366 | 1.03e-05 | |||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.03e-05
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| CH_jitterbug-like_rpt3 | cd21185 | third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
158-253 | 1.05e-05 | |||||||||||||
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409034 Cd Length: 98 Bit Score: 46.53 E-value: 1.05e-05
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
733-838 | 1.06e-05 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 46.93 E-value: 1.06e-05
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1512-1693 | 1.33e-05 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 48.98 E-value: 1.33e-05
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| CH_PLS1_rpt3 | cd21329 | third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
29-141 | 1.79e-05 | |||||||||||||
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.52 E-value: 1.79e-05
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| ClyA_Cry6Aa-like | cd22656 | Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1293-1480 | 1.83e-05 | |||||||||||||
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices. Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 49.68 E-value: 1.83e-05
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
3142-3184 | 2.99e-05 | |||||||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 43.36 E-value: 2.99e-05
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
1046-1602 | 3.80e-05 | |||||||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.80e-05
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| CH_FLNB_rpt2 | cd21313 | second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
149-252 | 5.52e-05 | |||||||||||||
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409162 Cd Length: 110 Bit Score: 45.08 E-value: 5.52e-05
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| CAMSAP_CH | pfam11971 | CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
160-239 | 7.00e-05 | |||||||||||||
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. Pssm-ID: 432229 Cd Length: 85 Bit Score: 43.83 E-value: 7.00e-05
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
954-1584 | 1.04e-04 | |||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.04e-04
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
3146-3182 | 1.22e-04 | |||||||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 41.72 E-value: 1.22e-04
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
959-1325 | 1.54e-04 | |||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.54e-04
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| CH_FLNA_rpt2 | cd21312 | second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
149-252 | 1.64e-04 | |||||||||||||
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409161 Cd Length: 114 Bit Score: 44.03 E-value: 1.64e-04
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| HEC1 | COG5185 | Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1161-1490 | 1.97e-04 | |||||||||||||
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.26 E-value: 1.97e-04
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| SPEC | smart00150 | Spectrin repeats; |
1281-1377 | 2.21e-04 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.09 E-value: 2.21e-04
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2778-2877 | 3.68e-04 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 42.69 E-value: 3.68e-04
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
587-1275 | 3.74e-04 | |||||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 3.74e-04
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| SPEC | cd00176 | Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1632-1793 | 4.72e-04 | |||||||||||||
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.36 E-value: 4.72e-04
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| CH_PLS2_rpt3 | cd21330 | third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
29-132 | 5.03e-04 | |||||||||||||
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409179 Cd Length: 125 Bit Score: 42.67 E-value: 5.03e-04
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| ZZ_Mind_bomb | cd02339 | Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ... |
3409-3455 | 5.28e-04 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster. Pssm-ID: 239079 Cd Length: 45 Bit Score: 40.13 E-value: 5.28e-04
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| CH_PLS1_rpt1 | cd21323 | first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
34-132 | 5.61e-04 | |||||||||||||
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409172 Cd Length: 145 Bit Score: 43.11 E-value: 5.61e-04
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| ZZ_dah | cd02345 | Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ... |
3409-3454 | 5.88e-04 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila. Pssm-ID: 239085 Cd Length: 49 Bit Score: 40.27 E-value: 5.88e-04
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| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1159-1458 | 6.11e-04 | |||||||||||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.11e-04
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
768-1473 | 7.10e-04 | |||||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 7.10e-04
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| SPEC | smart00150 | Spectrin repeats; |
1175-1273 | 8.71e-04 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.16 E-value: 8.71e-04
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1299-1606 | 9.38e-04 | |||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 9.38e-04
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2826-3130 | 1.43e-03 | |||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.43e-03
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1286-1378 | 1.60e-03 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 40.76 E-value: 1.60e-03
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
761-1585 | 2.33e-03 | |||||||||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.33e-03
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
728-1354 | 2.59e-03 | |||||||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.59e-03
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
1875-2077 | 2.75e-03 | |||||||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.75e-03
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2567-2663 | 2.80e-03 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.99 E-value: 2.80e-03
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| SPEC | smart00150 | Spectrin repeats; |
573-671 | 2.97e-03 | |||||||||||||
Spectrin repeats; Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.97e-03
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
2659-2763 | 2.97e-03 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.99 E-value: 2.97e-03
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| Spectrin | pfam00435 | Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1591-1693 | 4.02e-03 | |||||||||||||
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated. Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.61 E-value: 4.02e-03
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| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2572-2728 | 4.84e-03 | |||||||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.84e-03
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| SCP-1 | pfam05483 | Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1024-1444 | 5.86e-03 | |||||||||||||
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase. Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 5.86e-03
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| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
2587-2732 | 6.28e-03 | |||||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 6.28e-03
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
759-1169 | 6.40e-03 | |||||||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 6.40e-03
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| PRK10929 | PRK10929 | putative mechanosensitive channel protein; Provisional |
1293-1438 | 6.85e-03 | |||||||||||||
putative mechanosensitive channel protein; Provisional Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 6.85e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2571-3119 | 7.21e-03 | |||||||||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 7.21e-03
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